Biosorption is one such emerging technology which utilized naturally occurring waste materials to sequester heavy metals from polluted water. In the present study cinnamon was utilized for Cr(VI) removal from aqueous solutions.It was found that a time of two hours was sufficient for sorption to attain equilibrium. The optimum pH was 2 for Cr(VI) removal. Temprature has little influence on the biosorption process. The Cr(VI) removal decreased with increase in temperature. The biosorption data was well fitted to Dubinin - Radushkevich (D-R), Freundlich and Tempkin adsorption isotherm models, although the correlation coefficient of Langmuir model was high but the calculated adsorption capacity did not agree with the experimental. The thermodynamic study reveals that the biosorption process is spontaneous and the spontaneity decreased with temperature increase and the process is exothermic accompanied by highly ordered adsorbate at the solid liquid interface. ΔH°values were negative and lie in the range of physical adsorption.
CeruloplasminCP (EC1.16.3.1) activity has been assayed in (32) serum samples of patients with Chronic Renal Failure CRF, and (32) serum samples of healthy individuals without any clinically detectable diseases have been used as control group. The aim of this study is to measure CP activity and partially purifying the enzyme from sera of patients with CRF and healthy individuals. The results of this study revealed that CP activity of patient's serum shows a highly significant decrease (p < 0.05) compared to that of the healthy individuals. Ceruloplasmin enzyme was partially purified from the serum of patient with CRF and and healthy individual by three steps which operates throughout under mild conditions 4°, acetate buffer (pH 6.8): First step including the use of ammonium sulfate precipitation, second step utilize dialysis with acetate buffer, while the third step consists of gel-filtration on Sephacryl S200(27×1.6cm) . Insufficiently purified ceruloplasmin fractions obtained at various stages are diluted to the appropriate ionic strength and re-utilized. Two proteinous components had been isolated by gel filtration chromatography from the supernatant produced by ammonium sulfate.
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